SEG2_YEAST
ID SEG2_YEAST Reviewed; 1132 AA.
AC P34250; D6VXI3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Eisosome protein SEG2;
DE AltName: Full=Stability of eisosomes guaranteed protein 2;
GN Name=SEG2; OrderedLocusNames=YKL105C; ORFNames=YKL459;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8109175; DOI=10.1002/yea.320091113;
RA Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H.,
RA Bolotin-Fukuhara M., Sor F.;
RT "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of
RT Saccharomyces cerevisiae suggests the presence of a second aspartate
RT aminotransferase gene in yeast.";
RL Yeast 9:1259-1265(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-504; SER-507;
RP SER-556; SER-980 AND SER-1022, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=22869600; DOI=10.1083/jcb.201202097;
RA Moreira K.E., Schuck S., Schrul B., Frohlich F., Moseley J.B.,
RA Walther T.C., Walter P.;
RT "Seg1 controls eisosome assembly and shape.";
RL J. Cell Biol. 198:405-420(2012).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-526 AND LYS-743, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Likely plays only a minor role in eisosome assembly.
CC {ECO:0000269|PubMed:22869600}.
CC -!- SUBUNIT: Component of eisosomes, large cytoplasmic protein assemblies
CC that localize to specialized domains termed MCCs on the plasma
CC membrane. {ECO:0000269|PubMed:22869600}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22869600};
CC Peripheral membrane protein {ECO:0000269|PubMed:22869600}; Cytoplasmic
CC side {ECO:0000269|PubMed:22869600}. Note=Localizes to eisosomes.
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEG1 family. {ECO:0000305}.
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DR EMBL; X71133; CAA50452.1; -; Genomic_DNA.
DR EMBL; Z28105; CAA81945.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09053.1; -; Genomic_DNA.
DR PIR; S37932; S37932.
DR RefSeq; NP_012817.1; NM_001179671.1.
DR AlphaFoldDB; P34250; -.
DR SMR; P34250; -.
DR BioGRID; 34029; 138.
DR DIP; DIP-6273N; -.
DR IntAct; P34250; 3.
DR MINT; P34250; -.
DR STRING; 4932.YKL105C; -.
DR iPTMnet; P34250; -.
DR MaxQB; P34250; -.
DR PaxDb; P34250; -.
DR PRIDE; P34250; -.
DR TopDownProteomics; P34250; -.
DR EnsemblFungi; YKL105C_mRNA; YKL105C; YKL105C.
DR GeneID; 853756; -.
DR KEGG; sce:YKL105C; -.
DR SGD; S000001588; SEG2.
DR VEuPathDB; FungiDB:YKL105C; -.
DR HOGENOM; CLU_309545_0_0_1; -.
DR InParanoid; P34250; -.
DR OMA; SHEESHQ; -.
DR BioCyc; YEAST:G3O-31892-MON; -.
DR PRO; PR:P34250; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34250; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cell membrane; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1132
FT /note="Eisosome protein SEG2"
FT /id="PRO_0000203159"
FT REGION 76..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..645
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 743
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 1132 AA; 125593 MW; 013F55C2CCDD0F9D CRC64;
MIQESSPDAL AAAAAIGNAL SYNGRTVDKS KIPQYNQSFT SRTTSIAGIN RYTMLSNSRT
NSRMLLMNGN VRQYSKRTSS LPNQGHKNTS NNSAGRRQHR AHEDAETTFR EFGGKQSSKV
LNISSSTGQN SKSRTTSLGN SGSTIRTIKK YIPGPRGLMA VEVPVEVEPP RYSLSNRSNQ
RGGRAYSLPT RNNKTSLMHR NKTTKKAGSQ EKKSESGGKS KNDYHGKVLS KMHTTSLKQR
HNNVPLIPTT MNEETEQELQ EDLHDPLEFK PMIISDDENS FIEPSVLDRS IPKKDKSGLS
GREKKEEIET LLKEVHSLEE KISNIEIAKL NEEEREQSLI LELRKVKLDE ERRMELLKRE
LNIVKENADL EAQELKLIES KRKQHFHKGQ EVASEVKSIT IRQPTLSEPK PAYVPPEDVE
KEPSTLSNQT QNIENAENID SVDAEGNLVD PILLGSLNNS NFHMNSDNEV RCIADSNSLT
GSELSDYNYI EGSATDLRAT AKTSVESEIG GNQVGLKIPQ DDDSEKQEER TKGKKSGLVD
TNCFLVQKED QEEALSDNEP ESSEKFPSTS GIENVKLEDE TGSVMDKNNG PNNDKDDDDD
KDNDNDDDDD KDDDVNDDDK DENVDDDENV DDDDDDDDDD DDEYHDSYDV IMRDPVQIEQ
DISDVPSLKH PSEYSTETED NKKKEQNSEN AEVSQSGTNM AKYLRGANPY LTNTSSDTFS
LDSENVNSKS STDTTRVAPD LLKSSLQPQL RSDLKQSAVP SSTSSSIYSI ETSPNIDSST
GKTASNTKTN SHGPPTSISK QKYDQSSSHQ IPVMSPKRLD DKRKITNRSC LRTLRGSSNE
ATLSHNIVYP ASDSSSSPPY HSKKPSNPPS SGNLASHEAS KCFPKAPQAS TTSRRLPDHV
PLYIDKNNSA LYPKEPPARK SSFEKERPAK DNLGFRSMSL REPLITKNAT ATAAENLDVE
EKKEKGGHVS RKSWTFGLPS PLKRRTSHST HTTNETEIVN PMTNFKNKTN ENDMPILANK
KSCNNDDSSP YTASSMNTND VSEAGTEGHR FSLFGNKSQL SNRNISGGTA TLESSNPDLP
TALPLSVPVT IIDKNGEIHK LHNDDAAIKD KSHDRHGHSK FGRKLKKIFG RK
